Trans-feruloyl-CoA hydratase

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In enzymology, a trans-feruloyl-CoA hydratase (EC 4.2.1.101) is an enzyme that catalyzes the chemical reaction

4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA $\rightleftharpoons$ trans-feruloyl-CoA + H₂O

Hence, this enzyme has one substrate, 4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA, and two products, trans-feruloyl-CoA and H₂O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA hydro-lyase (trans-feruloyl-CoA-forming). This enzyme is also called trans-feruloyl-CoA hydro-lyase (incorrect).

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2J5I.

[edit] References

IUBMB entry for 4.2.1.101
BRENDA references for 4.2.1.101 (Recommended.)
PubMed references for 4.2.1.101
PubMed Central references for 4.2.1.101
Google Scholar references for 4.2.1.101
Narbad A, Gasson MJ (Pt 5). "Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens". Microbiology. 144: 1397–405. PMID 9611814.
Pometto AL 3rd Crawford DL (1983). "Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus". Appl. Environ. Microbiol. 45: 1582–5. PMID 6870241.